Glucose-6-phosphate dehydrogenase

Glucose-6-phosphate dehydrogenase (G6PDH; EC 1.1.1.49) is purified from a recombinant E. coli strain. G6PDH is a cytosolic enzyme that converts glucose-6-phosphate into 6-phosphoglucono-δ-lactone, the rate-limiting step of the pentose phosphate pathway, a metabolic pathway that supplies reducing energy to cells by maintaining the level of the co-enzyme nicotinamide adenine dinucleotide phosphate (NADPH). G6PDH is widely distributed in many species from bacteria to man. G6PDH is remarkable for its genetic diversity. Many variants of G6PDH, mostly produced from missense mutations, have been described with wide ranging levels of enzyme activity and associated clinical symptoms. G6PD deficiency is very common worldwide, and causes acute hemolytic anemia in the presence of simple infection, ingestion of fava beans, or reaction with certain medicines, antibiotics, antipyretics and antimalarials. The enzyme is supplied in 3.2 M ammonium sulphate. Activity: 1000 U/ml

Temperature and pH optimum/stability: The optimum pH and temperature are 7.5 and 25 °C, respectively.